ID D4ZM91_SHEVD Unreviewed; 672 AA.
AC D4ZM91;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=2,4-dienoyl-CoA reductase {ECO:0000313|EMBL:BAJ02790.1};
GN Name=fadH {ECO:0000313|EMBL:BAJ02790.1};
GN OrderedLocusNames=SVI_2819 {ECO:0000313|EMBL:BAJ02790.1};
OS Shewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 / DSS12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=637905 {ECO:0000313|EMBL:BAJ02790.1, ECO:0000313|Proteomes:UP000002350};
RN [1] {ECO:0000313|Proteomes:UP000002350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10179 / CIP 106290 / LMG 19151 / DSS12
RC {ECO:0000313|Proteomes:UP000002350};
RX PubMed=20458400; DOI=10.1039/c000396d;
RA Aono E., Baba T., Ara T., Nishi T., Nakamichi T., Inamoto E., Toyonaga H.,
RA Hasegawa M., Takai Y., Okumura Y., Baba M., Tomita M., Kato C., Oshima T.,
RA Nakasone K., Mori H.;
RT "Complete genome sequence and comparative analysis of Shewanella violacea,
RT a psychrophilic and piezophilic bacterium from deep sea floor sediments.";
RL Mol. Biosyst. 6:1216-1226(2010).
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR EMBL; AP011177; BAJ02790.1; -; Genomic_DNA.
DR RefSeq; WP_013052089.1; NC_014012.1.
DR AlphaFoldDB; D4ZM91; -.
DR STRING; 637905.SVI_2819; -.
DR KEGG; svo:SVI_2819; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG1902; Bacteria.
DR HOGENOM; CLU_012153_1_1_6; -.
DR OrthoDB; 8523426at2; -.
DR Proteomes; UP000002350; Chromosome.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd02930; DCR_FMN; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR001155; OxRdtase_FMN_N.
DR PANTHER; PTHR42917; 2,4-DIENOYL-COA REDUCTASE; 1.
DR PANTHER; PTHR42917:SF2; 2,4-DIENOYL-COA REDUCTASE [(2E)-ENOYL-COA-PRODUCING]; 1.
DR Pfam; PF00724; Oxidored_FMN; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000002350}.
FT DOMAIN 8..332
FT /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00724"
FT DOMAIN 378..643
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 672 AA; 73212 MW; 1B7DEEEC010537F5 CRC64;
MSNSYPHLMA PLDLGFRTIK NRSLMGSMHT NLEEAPNGFE RMAAYYAARA AGGIGMIVTG
GFAPNIEGGG MPNATMIATD EDIEQHRIIT QAVHKEDGVI CLQILHTGRY AYHPKLVSCS
PLQAPINQFV PRELDEAGIE KQIQDFVNCA LNSQKAGYDG VEIMGSEGYF INQFICKRTN
HRTDRWGGSY ENRTRLALEI VRRTREAVGE AFIIIFRLSM LDLVEGGSTW QEVVELAKGI
EKVGATIINT GVGWHEARVP TIATSVPRGA FVELTKRMKQ EVSIPLCTTN RINTPEVAEE
ILAQGNADIV SMARPMLADP DFMVKAQAGK SDEINTCIGC NQACLDHIFQ MKLVSCLVNP
QACHETELII KPTLEVKEIA VVGAGPAGLA AATTAARRGH KVTLFEAADK IGGQFNIAMQ
VPGKEEFSET IRYFNKQLEL TGVDVRLNTR ACEEDLIGFN EVLLATGIMP RQLDIPGINS
DKVLNYLDVL RDKKPVGKRV AIIGAGGIGF DVGEYLSHQG PSTSLDKDAY MKEWGVDLSG
STPGGLIEPQ CEPSPREIFL LQRKTSKVGA GLGKSTGWIH RTVLKNKGVK MLKGVHYHKI
DHEGLHISVD GEEQVLEVDN IIICAGQDSH RELQAKLEAN KVKVTLIGGA DIASELDAKR
AIKQGTEVAA AL
//
